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A6SUF7

- HEM1_JANMA

UniProt

A6SUF7 - HEM1_JANMA

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (21 Aug 2007)
      Previous versions | rss
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    • Comment

    Functioni

    Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).UniRule annotation

    Catalytic activityi

    L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei57 – 571NucleophileUniRule annotation
    Sitei109 – 1091Important for activityUniRule annotation
    Binding sitei119 – 1191SubstrateUniRule annotation
    Binding sitei130 – 1301SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi199 – 2046NADPUniRule annotation

    GO - Molecular functioni

    1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
    2. NADP binding Source: InterPro

    GO - Biological processi

    1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Porphyrin biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciJSP375286:GJ8U-214-MONOMER.
    UniPathwayiUPA00251; UER00316.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
    Short name:
    GluTRUniRule annotation
    Gene namesi
    Name:hemAUniRule annotation
    Ordered Locus Names:mma_0214
    OrganismiJanthinobacterium sp. (strain Marseille) (Minibacterium massiliensis)
    Taxonomic identifieri375286 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesOxalobacteraceaeJanthinobacterium
    ProteomesiUP000006388: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 429429Glutamyl-tRNA reductasePRO_0000335047Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi375286.mma_0214.

    Structurei

    3D structure databases

    ProteinModelPortaliA6SUF7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni56 – 594Substrate bindingUniRule annotation
    Regioni124 – 1263Substrate bindingUniRule annotation

    Domaini

    Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.UniRule annotation

    Sequence similaritiesi

    Belongs to the glutamyl-tRNA reductase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0373.
    HOGENOMiHOG000109650.
    KOiK02492.
    OMAiLAHKLTN.
    OrthoDBiEOG6MWNBM.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00087. Glu_tRNA_reductase.
    InterProiIPR000343. 4pyrrol_synth_GluRdtase.
    IPR015896. 4pyrrol_synth_GluRdtase_dimer.
    IPR015895. 4pyrrol_synth_GluRdtase_N.
    IPR018214. GluRdtase_CS.
    IPR016040. NAD(P)-bd_dom.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    [Graphical view]
    PfamiPF00745. GlutR_dimer. 1 hit.
    PF05201. GlutR_N. 1 hit.
    PF01488. Shikimate_DH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
    SUPFAMiSSF69075. SSF69075. 1 hit.
    SSF69742. SSF69742. 1 hit.
    TIGRFAMsiTIGR01035. hemA. 1 hit.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A6SUF7-1 [UniParc]FASTAAdd to Basket

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    MQLLAVGLNH TTAPVSLREK VAFPADQLGQ AVASARSWYG RSDATTYTDE    50
    AAILSTCNRT ELYAASNLPG GVNEAIDITA HFLADYHKLP YAELRPYLYA 100
    LPQDNAVRHA FRVASGLDSM VLGEPQILGQ MKDAVRQAEA AGGLGTYLHQ 150
    MFQRTFAVAK EVRSTTEIGA HSVSMAAASV RLSQRIFDKI SEQNVLFIGA 200
    GEMIELSATH FAAQNPKSVT IANRTLERGQ TLAHRFNGKA IRLADLPDQL 250
    ASYDIVISST ASSLPIIGLG MVERAIKARR HKPMFMVDLA VPRDIEAEIG 300
    RLDDVFLYTV DDLGSFVQTG VENRQAAVAQ AEAIIETRVR SFMHWIDARA 350
    VVPVIQDLHE SSETMRMIEL ERARKLLAKG EDIDAVLEAL SKGLTAKFLH 400
    GPQQALNNAQ GDERARLAAL LPQLFRTKR 429
    Length:429
    Mass (Da):47,029
    Last modified:August 21, 2007 - v1
    Checksum:iB22847099D3678CE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000269 Genomic DNA. Translation: ABR88801.1.
    RefSeqiWP_011979440.1. NC_009659.1.
    YP_001351904.1. NC_009659.1.

    Genome annotation databases

    EnsemblBacteriaiABR88801; ABR88801; mma_0214.
    GeneIDi5351794.
    KEGGimms:mma_0214.
    PATRICi22152829. VBIJanSp106498_0220.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000269 Genomic DNA. Translation: ABR88801.1 .
    RefSeqi WP_011979440.1. NC_009659.1.
    YP_001351904.1. NC_009659.1.

    3D structure databases

    ProteinModelPortali A6SUF7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 375286.mma_0214.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABR88801 ; ABR88801 ; mma_0214 .
    GeneIDi 5351794.
    KEGGi mms:mma_0214.
    PATRICi 22152829. VBIJanSp106498_0220.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109650.
    KOi K02492.
    OMAi LAHKLTN.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci JSP375286:GJ8U-214-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    HAMAPi MF_00087. Glu_tRNA_reductase.
    InterProi IPR000343. 4pyrrol_synth_GluRdtase.
    IPR015896. 4pyrrol_synth_GluRdtase_dimer.
    IPR015895. 4pyrrol_synth_GluRdtase_N.
    IPR018214. GluRdtase_CS.
    IPR016040. NAD(P)-bd_dom.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    [Graphical view ]
    Pfami PF00745. GlutR_dimer. 1 hit.
    PF05201. GlutR_N. 1 hit.
    PF01488. Shikimate_DH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
    SUPFAMi SSF69075. SSF69075. 1 hit.
    SSF69742. SSF69742. 1 hit.
    TIGRFAMsi TIGR01035. hemA. 1 hit.
    PROSITEi PS00747. GLUTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome analysis of Minibacterium massiliensis highlights the convergent evolution of water-living bacteria."
      Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D., Drancourt M.
      PLoS Genet. 3:1454-1463(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Marseille.

    Entry informationi

    Entry nameiHEM1_JANMA
    AccessioniPrimary (citable) accession number: A6SUF7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: August 21, 2007
    Last modified: October 1, 2014
    This is version 58 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA.UniRule annotation

    Keywords - Technical termi

    Complete proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3